Study of cosolvent-induced α-chymotrypsin fibrillogenesis: Does protein surface hydrophobicity trigger early stages of aggregation reaction?

The misfolding of specific proteins is often associated with their assembly into fibrillar aggregates, commonly termed amyloid fibrils. Despite the many efforts expended to characterize amyloid formation in vitro, there is no deep knowledge about the environment (in which aggregation occurs) as well as mechanism of this type of protein aggregation. Alpha-chymotrypsin was recently driven toward amyloid aggregation by the addition of intermediate concentrations of trifluoroethanol. In the present study, approaches such as turbidimetric, thermodynamic, intrinsic fluorescence and quenching studies as well as chemical modification have been successfully used to elucidate the underlying role of hydrophobic interactions (involved in early stages of amyloid formation) in α-chymotrypsin-based experimental system. © 2009 Springer Science+Business Media, LLC

Anti-amyloidogenic effect of AA3E2 attenuates β-amyloid induced toxicity in SK-N-MC cells

10.1016/j.cbi.2010.03.042Chemico-Biological Interactions186116-23CBIN

Inhibition of H2O2-induced neuroblastoma cell cytotoxicity by a triazine derivative, AA3E2

10.1016/j.ejphar.2009.07.017European Journal of Pharmacology6221-31-6EJPH